Related Experiment Video
Updated: Feb 5, 2026

07:26
Foraging Path-length Protocol for Drosophila melanogaster Larvae
Published on: April 23, 2016
9.9K
Seeing is believing: the Bicoid protein reveals its path
1Department of Experimental Medical Sciences, Lund University, BMC D10, S-22184 Lund, Sweden.
Hereditas
|September 18, 2018
Summary
The Bicoid (Bcd) morphogen gradient formation in Drosophila is re-evaluated. A new ARTS model explains Bcd localization via mRNA redistribution, challenging the older SDD model based on diffusion.
Area of Science:
- Developmental Biology
- Molecular Biology
- Genetics
Background:
- The Bicoid (Bcd) morphogen gradient in Drosophila is a long-standing model for pattern formation.
- The previously dominant Diffusion (SDD) model explained Bcd gradient formation through broad diffusion.
- Recent findings questioned the diffusion properties of Bcd, necessitating a revised model.
Purpose of the Study:
- To review recent findings on Bicoid (Bcd) morphogen gradient formation in Drosophila.
- To critically compare the established SDD model with the newer ARTS model.
- To elucidate the mechanisms and localization pathways of Bcd during early development.
Main Methods:
- Comparative analysis of existing models (SDD and ARTS) for Bcd gradient formation.
- Review of experimental evidence regarding Bcd movement and localization.
- Examination of mRNA redistribution and protein translation mechanisms.
Main Results:
- The SDD model, dominant for over two decades, faced challenges regarding Bcd diffusion properties.
- The ARTS model proposes gradient formation via mRNA redistribution along cortical microtubules.
- The ARTS model explains Bcd cortical movement and avoids assumptions of tip diffusion.
Conclusions:
- The ARTS model offers a more comprehensive explanation for Bcd gradient formation, addressing physical constraints of the SDD model.
- mRNA localization and translation are key to Bcd protein gradient formation in the ARTS model.
- Re-evaluation of Bcd localization pathways is crucial for understanding early Drosophila development.
More Related Videos
Related Concept Videos
Mean free path and Mean free time
5.2K
Consider the gas molecules in a cylinder. They move in a random motion as they collide with each other and change speed and direction. The average of all the path lengths between collisions is known as the "mean free path."
5.2K
Path Between Thermodynamics States
4.0K
Consider the two thermodynamic processes involving an ideal gas that are represented by paths AC and ABC in Figure 1:
4.0K
Interference: Path Lengths
2.2K
Consider two sources of sound, that may or may not be in phase, emitting waves at a single frequency, and consider the frequencies to be the same.
Two special sources may be considered when they are in phase. This can be easily achieved by feeding the two sources from the same source. An example would be synchronizing the two speakers by feeding them with the same source, such as the sound waves produced by a tuning fork. This setup ensures that the two sources have the same frequency and are...
Two special sources may be considered when they are in phase. This can be easily achieved by feeding the two sources from the same source. An example would be synchronizing the two speakers by feeding them with the same source, such as the sound waves produced by a tuning fork. This setup ensures that the two sources have the same frequency and are...
2.2K
Behavior of Gas Molecules: Molecular Diffusion, Mean Free Path, and Effusion
31.4K
Although gaseous molecules travel at tremendous speeds (hundreds of meters per second), they collide with other gaseous molecules and travel in many different directions before reaching the desired target. At room temperature, a gaseous molecule will experience billions of collisions per second. The mean free path is the average distance a molecule travels between collisions. The mean free path increases with decreasing pressure; in general, the mean free path for a gaseous molecule will be...
31.4K
Protein-protein Interfaces
14.7K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.7K
Protein and Protein Structure
87.9K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
87.9K

